Pages that link to "Q48806783"
Jump to navigation
Jump to search
The following pages link to Pathogenic mutations shift the equilibria of alpha-synuclein single molecules towards structured conformers (Q48806783):
Displaying 37 items.
- Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopy (Q21132346) (← links)
- Structures of the E46K mutant-type α-synuclein protein and impact of E46K mutation on the structures of the wild-type α-synuclein protein (Q22061749) (← links)
- Seeking a mechanism for the toxicity of oligomeric α-synuclein (Q28080551) (← links)
- Common features at the start of the neurodegeneration cascade (Q28483979) (← links)
- Understanding protein non-folding. (Q30385084) (← links)
- Are Charge-State Distributions a Reliable Tool Describing Molecular Ensembles of Intrinsically Disordered Proteins by Native MS? (Q30394019) (← links)
- Compaction properties of an intrinsically disordered protein: Sic1 and its kinase-inhibitor domain (Q30402284) (← links)
- Effect of spermidine on misfolding and interactions of alpha-synuclein (Q34291522) (← links)
- Familial Parkinson disease-associated mutations alter the site-specific microenvironment and dynamics of α-synuclein (Q35199433) (← links)
- Direct Detection of α-Synuclein Dimerization Dynamics: Single-Molecule Fluorescence Analysis (Q35529960) (← links)
- Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation (Q36384806) (← links)
- Structures and free energy landscapes of the wild-type and A30P mutant-type α-synuclein proteins with dynamics (Q36713739) (← links)
- Initiation of assembly of tau(273-284) and its ΔK280 mutant: an experimental and computational study. (Q36874806) (← links)
- Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics (Q37026033) (← links)
- α-Synuclein misfolding assessed with single molecule AFM force spectroscopy: effect of pathogenic mutations (Q37351690) (← links)
- Naturally occurring mutations alter the stability of polycystin-1 polycystic kidney disease (PKD) domains (Q37432198) (← links)
- Understanding biology by stretching proteins: recent progress. (Q37688543) (← links)
- Multicolor single-molecule FRET to explore protein folding and binding (Q37770057) (← links)
- Nanoimaging for protein misfolding diseases (Q37776219) (← links)
- Nanoimaging for prion related diseases (Q37781245) (← links)
- Biophysical groundwork as a hinge to unravel the biology of α-synuclein aggregation and toxicity (Q38180144) (← links)
- Single-molecule force spectroscopy reveals the individual mechanical unfolding pathways of a surface layer protein (Q38334135) (← links)
- Biophysical Methods to Investigate Intrinsically Disordered Proteins: Avoiding an "Elephant and Blind Men" Situation (Q38589803) (← links)
- Amyloid misfolding, aggregation, and the early onset of protein deposition diseases: insights from AFM experiments and computational analyses (Q39004129) (← links)
- Conformational templating of α-synuclein aggregates in neuronal-glial cultures (Q41494001) (← links)
- Alteration of the alpha-synuclein folding landscape by a mutation related to Parkinson's disease (Q41905102) (← links)
- Mechanical resistance in unstructured proteins. (Q42077482) (← links)
- Single-molecule fluorescence studies of intrinsically disordered proteins. (Q46033026) (← links)
- Single-molecule assays for investigating protein misfolding and aggregation (Q46164744) (← links)
- Comparison of the in vivo induction and transmission of α-synuclein pathology by mutant α-synuclein fibril seeds in transgenic mice (Q47647268) (← links)
- Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology (Q48175839) (← links)
- A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides (Q50125039) (← links)
- Alpha-synuclein oligomers and fibrils originate in two distinct conformer pools: a small angle X-ray scattering and ensemble optimisation modelling study (Q57982348) (← links)
- Age-dependent accumulation of oligomeric SNCA/α-synuclein from impaired degradation in mutant LRRK2 knockin mouse model of Parkinson disease: role for therapeutic activation of chaperone-mediated autophagy (CMA) (Q64768798) (← links)
- Localized Induction of Wild-Type and Mutant Alpha-Synuclein Aggregation Reveals Propagation along Neuroanatomical Tracts (Q64866037) (← links)
- Single-molecule mechanical unfolding of amyloidogenic beta2-microglobulin: the force-spectroscopy approach (Q83999161) (← links)
- Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity (Q96135531) (← links)